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Protein Glycosylation

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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Related Experiment Video

Updated: Jun 8, 2026

The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides

The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides

Published on: November 2, 2021

Systems analysis of bacterial glycomes.

Emily Kay¹, Victor I Lesk, Alireza Tamaddoni-Nezhad

¹The Centre for Integrative Systems Biology, Imperial College, London SW7 2AZ, UK.

Biochemical Society Transactions

|September 25, 2010

Summary

Advancements in genomics and mass spectrometry (MS) analysis enable bacterial glycomics research. This study integrates bioinformatic and experimental methods to understand Campylobacter jejuni glycan structures and functions.

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Glycan Node Analysis: A Bottom-up Approach to Glycomics

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

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Last Updated: Jun 8, 2026

The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides

The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides

Published on: November 2, 2021

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

Area of Science:

Microbiology
Glycobiology
Bioinformatics

Background:

Bacteria synthesize diverse cell-surface glycans crucial for pathogenesis and survival.
Studying bacterial glycans is challenging due to combinatorial complexity and limited genetic data.
Genomics and advanced MS have revolutionized bacterial glycomics.

Purpose of the Study:

To explore novel glycan structures and their functions in bacteria.
To integrate bioinformatic predictions with experimental validation for gene function assignment.
To exemplify advances in bacterial glycomics using Campylobacter jejuni.

Main Methods:

Genomic analysis and high-throughput mass spectrometry (MS).
Bioinformatic analysis of predicted glycan biosynthetic pathways.
Systematic gene mutagenesis and functional analysis.
Structural analysis using MS and Nuclear Magnetic Resonance (NMR) spectroscopy.

Main Results:

Identification of novel bacterial glycan structures.
Successful assignment of genetic information to glycan structures.
Demonstration of systems-level analysis for predicting gene function.
Experimental confirmation of predicted gene functions in Campylobacter jejuni.

Conclusions:

Integrated bioinformatic and experimental approaches are essential for deciphering bacterial glycan biosynthesis and function.
Advances in technology facilitate glycoprospecting and glycoengineering.
This study provides a framework for understanding the role of glycans in bacterial pathogenesis.